1208228-64-1Relevant articles and documents
2,4-Diaminopyrimidine MK2 inhibitors. Part II: Structure-based inhibitor optimization
Harris, Christopher M.,Ericsson, Anna M.,Argiriadi, Maria A.,Barberis, Claude,Borhani, David W.,Burchat, Andrew,Calderwood, David J.,Cunha, George A.,Dixon, Richard W.,Frank, Kristine E.,Johnson, Eric F.,Kamens, Joanne,Kwak, Silvia,Li, Biqin,Mullen, Kelly D.,Perron, Denise C.,Wang, Lu,Wishart, Neil,Wu, Xiaoyun,Zhang, Xiaolei,Zmetra, Tami R.,Talanian, Robert V.
, p. 334 - 337 (2010)
We describe structure-based optimization of a series of novel 2,4-diaminopyrimidine MK2 inhibitors. Co-crystal structures (see accompanying Letter) demonstrated a unique inhibitor binding mode. Resulting inhibitors had IC50 values as low as 19 nM and moderate selectivity against a kinase panel. Compounds 15, 31a, and 31b inhibit TNFα production in peripheral human monocytes.
